ArticleBiophysical journal2007
Protein geometry and placement in the cardiac dyad influence macroscopic properties of calcium-induced calcium release.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 63 citations in OpenAlex.
- Calcium dynamics in small spaces: Lessons learned from modeling in dendritic spines.Biophysical journal · 2025Review
- Novel Ca2+ wave mechanisms in cardiac myocytes revealed by multiscale Ca2+ release model.The Journal of general physiology · 2025Article
- Phosphorylation of RyR2 simultaneously expands the dyad and rearranges the tetramers.The Journal of general physiology · 2024Article
- Nernst-Planck-Gaussian finite element modelling of CaFrontiers in physiology · 2024Article
- CaJournal of molecular and cellular cardiology · 2023Article
- Endoplasmic Reticulum-Plasma Membrane Junctions as Sites of Depolarization-Induced CaAnnual review of physiology · 2023Review
- Close agreement between deterministic versus stochastic modeling of first-passage time to vesicle fusion.Biophysical journal · 2022Article
- Co-localization and confinement of ecto-nucleotidases modulate extracellular adenosine nucleotide distributions.PLoS computational biology · 2020Article
- Article
- 3D dSTORM imaging reveals novel detail of ryanodine receptor localization in rat cardiac myocytes.The Journal of physiology · 2019Article
- Mechanisms of the cyclic nucleotide cross-talk signaling network in cardiac L-type calcium channel regulation.Journal of molecular and cellular cardiology · 2017Article
- Studying dyadic structure-function relationships: a review of current modeling approaches and new insights into CaClinical Medicine Insights. Cardiology · 2017Article
- Ultrastructural Analysis of Self-Associated RyR2s.Biophysical journal · 2016Article
- On the Adjacency Matrix of RyR2 Cluster Structures.PLoS computational biology · 2015Article
- A multiscale computational model of spatially resolved calcium cycling in cardiac myocytes: from detailed cleft dynamics to the whole cell concentration profiles.Frontiers in physiology · 2015Article
- The ryanodine receptor patchwork: knitting calcium spark dynamics.Biophysical journal · 2014Article
- Computational modeling of subcellular transport and signaling.Current opinion in structural biology · 2014Review
- Ca2+ channel nanodomains boost local Ca2+ amplitude.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Ultrastructural remodelling of Ca(2+) signalling apparatus in failing heart cells.Cardiovascular research · 2012Article
- A theory of biological relativity: no privileged level of causation.Interface focus · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
In cardiac ventricular myocytes, events crucial to excitation-contraction coupling take place in spatially restricted microdomains known as dyads. The movement and dynamics of calcium (Ca2+) ions in the dyad have often been described by assigning continuously valued Ca2+ concentrations to one or more dyadic compartments. However, even at its peak, the estimated number of free Ca2+ ions present in a single dyad is small (approximately 10-100 ions). This in turn suggests that modeling dyadic calcium dynamics using laws of mass action may be inappropriate. In this study, we develop a model of stochastic molecular signaling between L-type Ca2+ channels (LCCs) and ryanodine receptors (RyR2s) that describes: a), known features of dyad geometry, including the space-filling properties of key dyadic proteins; and b), movement of individual Ca2+ ions within the dyad, as driven by electrodiffusion. The model enables investigation of how local Ca2+ signaling is influenced by dyad structure, including the configuration of key proteins within the dyad, the location of Ca2+ binding sites, and membrane surface charges. Using this model, we demonstrate that LCC-RyR2 signaling is influenced by both the stochastic dynamics of Ca2+ ions in the dyad as well as the shape and relative positioning of dyad proteins. Results suggest the hypothesis that the relative placement and shape of the RyR2 proteins helps to "funnel" Ca2+ ions to RyR2 binding sites, thus increasing excitation-contraction coupling gain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.